Tag | Content |
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CPLM ID | CPLM-009785 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Uncharacterized Nudix hydrolase YfcD |
Protein Synonyms/Alias | |
Gene Name | yfcD |
Gene Synonyms/Alias | b2299; JW2296 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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111 | GQFYFEDKNCRVWGA | acetylation | [1] | 159 | EFTPDSLKALALWMK | acetylation | [1] | 166 | KALALWMKRNAKNEA | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | |
Sequence Annotation | DOMAIN 35 163 Nudix hydrolase. MOTIF 72 94 Nudix box. METAL 88 88 Magnesium. METAL 92 92 Magnesium (By similarity). |
Keyword | 3D-structure; Complete proteome; Hydrolase; Magnesium; Metal-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 180 AA |
Protein Sequence | MEQRRLASTE WVDIVNEENE VIAQASREQM RAQCLRHRAT YIVVHDGMGK ILVQRRTETK 60 DFLPGMLDAT AGGVVQADEQ LLESARREAE EELGIAGVPF AEHGQFYFED KNCRVWGALF 120 SCVSHGPFAL QEDEVSEVCW LTPEEITARC DEFTPDSLKA LALWMKRNAK NEAVETETAE 180 |
Gene Ontology | GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |